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3S1Y

AMP-C BETA-LACTAMASE (PSEUDOMONAS AERUGINOSA) in complex with a beta-lactamase inhibitor

Functional Information from GO Data
ChainGOidnamespacecontents
A0008800molecular_functionbeta-lactamase activity
A0016787molecular_functionhydrolase activity
A0017001biological_processantibiotic catabolic process
A0030288cellular_componentouter membrane-bounded periplasmic space
A0042597cellular_componentperiplasmic space
A0046677biological_processresponse to antibiotic
Functional Information from PDB Data
site_idAC1
Number of Residues25
DetailsBINDING SITE FOR RESIDUE S1Y A 398
ChainResidue
AGLY89
ATYR249
AALA319
ALYS342
ATHR343
AGLY344
ASER345
ATHR346
AASN373
AIPA400
AHOH1020
ASER90
AHOH1077
AHOH1113
AHOH1174
AHOH1219
AHOH1301
AHOH1373
AGLN146
ATYR177
AASN179
AVAL239
AGLY240
APRO241
AGLY242

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 399
ChainResidue
AGLN146
APHE147
AASN179
AHOH1032

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE IPA A 400
ChainResidue
ATHR316
AALA319
AS1Y398
AHOH1091

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE IPA A 401
ChainResidue
AGLU269
AALA276
AASP280
AGLN321
APRO322
AHOH1300

Functional Information from PROSITE/UniProt
site_idPS00336
Number of Residues8
DetailsBETA_LACTAMASE_C Beta-lactamase class-C active site. FEIGSVSK
ChainResidueDetails
APHE86-LYS93

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Acyl-ester intermediate => ECO:0000255|PROSITE-ProRule:PRU10102
ChainResidueDetails
ASER90

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000250
ChainResidueDetails
ATYR177

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
ALYS342

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PDB entries from 2024-07-10

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